Laughrea M, Tam J
Lady Davis Institute for Medical Research, Sir Mortimer B. Davis--Jewish General Hospital, Montreal, Quebec, Canada.
Biochemistry. 1991 Dec 3;30(48):11412-20. doi: 10.1021/bi00112a007.
We have studied the effect of the binding of ribosomal protein S1 and initiation factor IF3 on the accessibility of nucleotide residues 584-1506 in the small subunit of the Escherichia coli ribosome. Protein S1 strongly decreases RNase V1 attack at G1164, in hairpin 40 of the 3' major domain, and weakly decreases DMS attack at C1302, in the central loop of the 3' major domain, and at A1503, in the 3' minor domain. It also weakly increases the DMS reactivity of A1004, in the 3' major domain, and of A901, in the central domain. Factor IF3 strongly decreases RNase V1 attack (but not dimethyl sulfate attack) at A1408, in the decoding site, and weakly protects A1500, in the 3' minor domain and near the colicin E3 cleavage site. Neomycin does not interfere with this effect of IF3, but IF3 interferes with the protective effect of neomycin against dimethyl sulfate attack at A1408.
我们研究了核糖体蛋白S1和起始因子IF3的结合对大肠杆菌核糖体小亚基中核苷酸残基584 - 1506可及性的影响。蛋白S1强烈降低了3' 主要结构域的发夹40中G1164处的核糖核酸酶V1攻击，并且微弱降低了3' 主要结构域的中心环中C1302处以及3' 次要结构域中A1503处的硫酸二甲酯攻击。它还微弱增加了3' 主要结构域中A1004以及中心结构域中A901的硫酸二甲酯反应性。因子IF3强烈降低了解码位点处A1408的核糖核酸酶V1攻击（但不降低硫酸二甲酯攻击），并且微弱保护了3' 次要结构域中靠近大肠杆菌素E3切割位点的A1500。新霉素不干扰IF3的这种作用，但IF3干扰了新霉素对A1408处硫酸二甲酯攻击的保护作用。
